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Initial assessment of α-synuclein structure in platelets

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Abstract

Over the last few years data from our group have indicated that α-synuclein is important in development of immune cells as well as potentially erythrocytes and platelets. The latter is important since this protein may work as negative regulator of granule release. Thus, we sought to begin to understand the structure of this protein in platelets. Flow cytometric analysis of this protein using region-specific (N-terminus, central region and C-terminus) monoclonal antibodies was performed. Antibody to the central region gave the strongest shift among all three antibodies, with the C-terminus having intermediate shift and N-terminus minimal shift. Western blotting using the same antibodies showed similar binding of all antibodies to α-synuclein. These results suggest a similar arrangement of this protein in platelets as seen in neurons. Future studies ought to look at the role that each protein region plays in platelets.

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Acknowledgements

This study was supported by grant funding from the Office of Diversity and Inclusion of the University Hospitals Cleveland Medical Center awarded to R.W.M. The authors acknowledge technological and logistical assistance provided by Ms. Nancy Nagy at CWRU supported by NIH R01 AI034343 Grant (awarded to C.V.H).

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Correspondence to Robert W. Maitta.

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Stefaniuk, C.M., Schlegelmilch, J., Meyerson, H.J. et al. Initial assessment of α-synuclein structure in platelets. J Thromb Thrombolysis 53, 950–953 (2022). https://doi.org/10.1007/s11239-021-02607-z

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